Study of catalase immobilized on a silicate matrix for non-aqueous biocatalysis

Catalytic activity of catalase (CAT) immobilized on a modified silicate matrix to mediate decomposition of meta-chloroperoxibenzoic acid (3-CPBA) in acetonitrile has been investigated by means of quantitative UV-spectrophotometry. Under the selected experimental conditions, the kinetic parameters: the apparent Michaelis constat (KM), the apparent maximum rate of enzymatic reaction (Vmaxapp), the first order specific rate constants (ksp), the energy of activation (Ea) and the pre-exponential factor of the Arrhenius equation (Z0) were calculated. Conclusions regarding the rate-limiting step of the overall catalytic process were drawn from the calculated values of the Gibbs energy of activation ΔG*, the enthalpy of activation ΔH*, and the entropy of activation ΔS*.